Publications of Ilme Schlichting

Blumenstein, L.; Domratcheva, T.; Niks, D.; Ngo, H.; Seidel, R.; Dunn, M. F.; Schlichting, I.: βQ114N and βT110V Mutations Reveal a Critically Important Role of the Substrate α-Carboxylate Site in the Reaction Specificity of Tryptophan Synthase. Biochemistry 46 (49), 1, pp. 14100 - 14116 (2007)

Ngo, H.; Harris, R.; Kimmich, N.; Casino, P.; Niks, D.; Blumenstein, L.; Barends, T. R.; Kulik, V.; Weyand, M.; Schlichting, I. et al.; Dunn, M. F.: Synthesis and Characterization of Allosteric Probes of Substrate Channeling in the Tryptophan Synthase Bienzyme Complex. Biochemistry 46 (26), 1, pp. 7713 - 7727 (2007)

Blankenfeldt, W.; Thomä, N. H.; Wray, J. S.; Gautel, M.; Schlichting, I.: Crystal structures of human cardiac β-myosin II S2-Δ provide insight into the functional role of the S2 subfragment. Proceedings of the National Academy of Sciences of the USA 103 (47), 1, pp. 17713 - 17717 (2006)

Kühnel, K.; Blankenfeldt, W.; Terner, J.; Schlichting, I.: Crystal Structures of Chloroperoxidase with Its Bound Substrates and Complexed with Formate, Acetate, and Nitrate. Journal of Biological Chemistry 281 (33), 1, pp. 23990 - 23998 (2006)

Kühnel, K.; Veltel, S.; Schlichting, I.; Wittinghofer, A.: Crystal Structure of the Human Retinitis Pigmentosa 2 Protein and Its Interaction with Arl3. Structure 14 (2), 1, pp. 367 - 378 (2006)

Kulik, V.; Hartmann, E.; Weyand, M.; Frey, M.; Gierl, A.; Niks, D.; Dunn, M. F.; Schlichting, I.: On the Structural Basis of the Catalytic Mechanism and the Regulation of the Alpha Subunit of Tryptophan Synthase from Salmonella typhimurium and BX1 from Maize, Two Evolutionarily Related Enzymes. Journal of Molecular Biology 352 (3), 1, pp. 608 - 620 (2005)

Kühnel, K.; Jarchau, T.; Wolf, E.; Schlichting, I.; Ulrich, W.; Wittinghofer, A.; Strelkov, S. V.: The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat. Proceedings of the National Academy of Sciences of the United States of America 101 (49), 1, pp. 17027 - 17032 (2004)

Wade, R. C.; Winn, P. J.; Schlichting, I.; Sudarko, S.: A survey of active site access channels in cytochromes P450. Journal of Inorganic Biochemistry 98 (7), 1, pp. 1175 - 1182 (2004)

Fedorov, R.; Vasan, R.; Ghosh, D. K.; Schlichting, I.: Structures of nitric oxide synthase isoforms complexed with the inhibitor AR-R17477 suggest a rational basis for specificity and inhibitor design. Proceedings of the National Academy of Sciences of the United States of America 101 (16), 1, pp. 5892 - 5897 (2004)

Pylypenko, O.; Vitali, F.; Zerbe, K.; Robinson, J. A.; Schlichting, I.: Crystal structure of OxyC, a cytochrome P450 implicated in an oxidative C-C coupling reaction during vancomycin biosynthesis. Journal of Biological Chemistry 278 (47), 1, pp. 46727 - 46733 (2003)

Fedorov, R.; Ghosh, D. K.; Schlichting, I.: Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase - structural models of the short-lived oxygen complexes. Archives of Biochemistry and Biophysics 409 (1), 1, pp. 25 - 31 (2003)

Fedorov, R.; Hartmann, E.; Ghosh, D. K.; Schlichting, I.: Structural basis for the specificity of the nitric-oxide synthase inhibitors W1400 and N^ω-propyl-L-Arg for the inducible and neuronal isoforms. Journal of Biological Chemistry 278 (46), 1, pp. 45818 - 45825 (2003)

Fedorov, R.; Schlichting, I.; Hartmann, E.; Domratcheva, T.; Fuhrmann, M.; Hegemann, P.: Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii. Biophysical Journal 84 (4), 1, pp. 2474 - 2482 (2003)

Kottke, T.; Dick, B.; Fedorov, R.; Schlichting, I.; Deutzmann, R.; Hegemann, P.: Irreversible photoreduction of flavin in a mutated Phot-LOV1 domain. Biochemistry 42 (33), 1, pp. 9854 - 9862 (2003)

Pylypenko, O.; Rak, A.; Reents, R.; Niculae, A.; Sidorovitch, V.; Cioaca, M.-D.; Bessolitsyna, E.; Thomä, N. H.; Waldmann, H.; Schlichting, I. et al.; Goody, R. S.; Alexandrov, K.: Structure of rab escort protein-1 in complex with Rab geranylgeranyltransferase. Molecular Cell 11 (2), 1, pp. 483 - 494 (2003)

Zerbe, K.; Pylypenko, O.; Vitali, F.; Zhang, W.; Rouset, S.; Heck, M.; Vrijbloed, J. W.; Bischoff, D.; Bister, B.; Süssmuth, R. D. et al.; Pelzer, S.; Wohlleben, W.; Robinson, J. A.; Schlichting, I.: Crystal Structure of OxyB, a Cytochrome P450 Implicated in an Oxidative Phenol Coupling Reaction during Vancomycin Biosynthesis. Journal of Biological Chemistry 277 (49), 1, pp. 47476 - 47485 (2002)

Kulik, V.; Weyand, M.; Seidel, R.; Niks, D.; Arac, D.; Dunn, M. F.; Schlichting, I.: On the role of αThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase. Journal of Molecular Biology 324 (4), 1, pp. 677 - 690 (2002)

Weyand, M.; Schlichting, I.; Herde, P.; Marabotti, A.; Mozzarelli, A.: Crystal structure of the βSer¹⁷⁸ -> Pro mutant of tryptophan synthase - A "knock-out" allosteric enzyme. Journal of Biological Chemistry 277 (12), 1, pp. 10653 - 10660 (2002)

Weyand, M.; Schlichting, I.; Marabotti, A.; Mozzarelli, A.: Crystal structures of a new class of allosteric effectors complexed to tryptophan synthase. Journal of Biological Chemistry 277 (12), 1, pp. 10647 - 10652 (2002)

Groot, M.-L.; Vos, M. H.; Schlichting, I.; van Mourik, F.; Joffre, M.; Lambry, J.-C.; Martin, J.-L.: Coherent infrared emission from myoglobin crystals: An electric field measurement. Proceedings of the National Academy of Sciences of the United States of America 99 (3), 1, pp. 1323 - 1328 (2002)